Iron in PDB 6oxj: X-Ray Crystal Structure of Y140F FTMOX1 Bound to Fe(II)

All present enzymatic activity of X-Ray Crystal Structure of Y140F FTMOX1 Bound to Fe(II):
1.14.11.38;

The structure of X-Ray Crystal Structure of Y140F FTMOX1 Bound to Fe(II), PDB code: 6oxj was solved by N.P.Dunham, A.K.Boal, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	59.37 / 1.55
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	73.884, 78.069, 91.444, 90.00, 90.00, 90.00
R / Rfree (%)	21.3 / 24

The binding sites of Iron atom in the X-Ray Crystal Structure of Y140F FTMOX1 Bound to Fe(II) (pdb code 6oxj). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the X-Ray Crystal Structure of Y140F FTMOX1 Bound to Fe(II), PDB code: 6oxj:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the X-Ray Crystal Structure of Y140F FTMOX1 Bound to Fe(II)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of X-Ray Crystal Structure of Y140F FTMOX1 Bound to Fe(II) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe301 b:16.2 occ:0.50 O A:HOH413 2.0 15.2 1.0 O A:HOH468 2.0 17.4 1.0 O A:HOH437 2.2 16.7 1.0 OD1 A:ASP131 2.2 15.5 1.0 NE2 A:HIS129 2.3 14.1 1.0 NE2 A:HIS205 2.4 12.3 1.0 CG A:ASP131 3.1 15.4 1.0 CE1 A:HIS129 3.3 14.2 1.0 CE1 A:HIS205 3.3 12.3 1.0 CD2 A:HIS129 3.3 14.1 1.0 CD2 A:HIS205 3.3 12.1 1.0 OD2 A:ASP131 3.3 15.7 1.0 ND1 A:HIS129 4.4 14.0 1.0 ND1 A:HIS205 4.4 12.0 1.0 CG A:HIS129 4.4 14.0 1.0 CG A:HIS205 4.4 11.9 1.0 OE1 A:GLN126 4.5 17.5 1.0 CB A:ASP131 4.6 15.0 1.0 OH A:TYR224 4.7 14.1 1.0 CA A:ASP131 5.0 14.8 1.0

Iron binding site 2 out of 2 in the X-Ray Crystal Structure of Y140F FTMOX1 Bound to Fe(II)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of X-Ray Crystal Structure of Y140F FTMOX1 Bound to Fe(II) within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe301 b:14.1 occ:0.50 O B:HOH429 2.0 15.2 1.0 O B:HOH504 2.0 16.9 1.0 OD1 B:ASP131 2.1 14.3 1.0 O B:HOH497 2.3 18.7 1.0 NE2 B:HIS205 2.4 12.3 1.0 NE2 B:HIS129 2.4 13.9 1.0 CG B:ASP131 3.0 14.2 1.0 CE1 B:HIS205 3.3 12.2 1.0 OD2 B:ASP131 3.3 14.3 1.0 CD2 B:HIS129 3.3 14.0 1.0 CD2 B:HIS205 3.4 12.2 1.0 CE1 B:HIS129 3.4 14.0 1.0 OH B:TYR224 4.2 13.1 1.0 ND1 B:HIS205 4.4 12.1 1.0 CB B:ASP131 4.4 14.0 1.0 CG B:HIS205 4.5 12.1 1.0 ND1 B:HIS129 4.5 13.8 1.0 CG B:HIS129 4.5 13.8 1.0 OE1 B:GLN126 4.7 24.0 1.0 CA B:ASP131 4.8 13.8 1.0 N B:ASP131 5.0 13.4 1.0

N.P.Dunham, J.M.Del Rio Pantoja, B.Zhang, L.J.Rajakovich, B.D.Allen, C.Krebs, A.K.Boal, J.M.Bollinger Jr.. Hydrogen Donation But Not Abstraction By A Tyrosine (Y68) During Endoperoxide Installation By Verruculogen Synthase (FTMOX1). J.Am.Chem.Soc. V. 141 9964 2019.
ISSN: ESSN 1520-5126
PubMed: 31117657
DOI: 10.1021/JACS.9B03567